Thiolases of Escherichia coli: purification and chain length specificities.
J Bacteriol, 1975/5;122(2):407-11.
PMID: 236278
Impact factor: 3.476
Abstract
The presence of only one thiolase (EC 2.3.1.9) in wild-type Escherichia coli induced for enzymes of beta oxidation was demonstrated. A different thiolase was shown to be present in a mutant constitutive for the enzymes of butyrate degradation. The two thiolases were purified to near homogeneity by a simple two-step procedure and were found to be associated with different proteins as shown by gel electrophoresis. The thiolase isolated from induced wild-type Escherichia coli cell was active on beta-ketoacyl-coenzyme A derivatives containing 4 to 16 carbons, but exhibited optimal activity with medium-chain substrates. In contrast, the thiolase isolated from the constitutive mutant was shown to be specific for acetoacetyl-coenzyme A.
MeSH terms
Acetyl-CoA C-Acetyltransferase; Acetyltransferases; Butyrates; Cell Fractionation; Chromatography; Coenzyme A; Electrophoresis, Disc; Escherichia coli; Fatty Acids; Hot Temperature; Isoenzymes; Oxidation-Reduction
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